Modomics - A Database of RNA Modifications

ID Card:

Full name: Methylenetetrahydrofolate--tRNA-(uracil-54-)-methyltransferase TrmFO
Synonym: Gid, YlyC
GI: 3183519
Orf: BSU16130
COG: COG1206
UniProt: P39815
Alpha Fold Predicted Structure: AF-P39815-F1
Enzyme type: methyltransferase
Position of modification - modification: t:54 - m5U



Protein sequence:

MNQQTVNVIGAGLAGSEAAWQLAKRGIQVKLYEMRPVKQTPAHHTDKFAELVCSNSLRSNTLANAVGVLKEEMRALDSAIIAAADECSVPAGGALAVDRHEFAASVTNRVKNHPNVTVINEEVTEIPEGPTIIATGPLTSESLSAQLKELTGEDYLYFYDAAAPIVEKDSLDMDKVYLKSRYDKGEAAYLNCPMTEEEFDRFHEALTSAETVPLKEFEKEIFFEGCMPIEVMAKRGKKTMLFGPMKPVGLEHPVTGKRPYAVVQLRQDDAAGTLYNIVGFQTHLKWGDQKEVLKLIPGLENVEIVRYGVMHRNTFINSPSLLKPTYQFKNRSDLFFAGQMTGVEGYVESAASGLVAGINAAKLVLGEELVIFPQETAIGSMAHYITTTNQKNFQPMNANFGLLKELPVKIKNKKERNEQYANRAIETIQTISKTI

Comments:

In all Eukarya and many Gram-negative Bacteria, the methyl donor for this reaction is S-adenosyl-L-methionine (S-AdoMet), while in several Gram-positive Bacteria, the source of carbon is N5, N10-methylenetetrahydrofolate (CH2H4folate) . Modification in position 54 has been mapped in all tRNAs( Urbonavičius et al. 2005). Enzymatic reactions has been mapped to the MODOMICS RNA dataset. Therefore, more tRNA isoacepptors could be available.





Alpha Fold Predicted Structure:




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Protein sequence:

M N Q Q T V N V I G A G L A G S E A A W Q L A K R G I Q V K L Y E M R P V K Q T P A H H T D K F A E L V C S N S L R S N T L A N A V G V L K E E M R A L D S A I I A A A D E C S V P A G G A L A V D R H E F A A S V T N R V K N H P N V T V I N E E V T E I P E G P T I I A T G P L T S E S L S A Q L K E L T G E D Y L Y F Y D A A A P I V E K D S L D M D K V Y L K S R Y D K G E A A Y L N C P M T E E E F D R F H E A L T S A E T V P L K E F E K E I F F E G C M P I E V M A K R G K K T M L F G P M K P V G L E H P V T G K R P Y A V V Q L R Q D D A A G T L Y N I V G F Q T H L K W G D Q K E V L K L I P G L E N V E I V R Y G V M H R N T F I N S P S L L K P T Y Q F K N R S D L F F A G Q M T G V E G Y V E S A A S G L V A G I N A A K L V L G E E L V I F P Q E T A I G S M A H Y I T T T N Q K N F Q P M N A N F G L L K E L P V K I K N K K E R N E Q Y A N R A I E T I Q T I S K T I
50100150200250300350400SequenceGHTBSN

Secondary Structure Alphabet

  • G: 3-turn helix (310helix)
  • H: α-helix
  • I: 𝝅-helix (5 - turn helix)
  • T: Hydrogen Bonded Turn
  • B: β-sheet
  • S: Bend
  • C: Coil (residues not present in any of the above conformations)
  • N: Not assigned

Download PDB Structures & DSSP Secondary Structures:

Alpha Fold Pdb Files   AF-P39815-F1.pdb  
Alpha Fold Pdbx/mmCIF Files   AF-P39815-F1.cif  
DSSP Secondary Structures   P39815.dssp  





Publications:

Links:

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